The �\-amylase encoding gene from acidophilic bacterium Bacillus acidicola was cloned into pET28a(+) vector and expressed in Escherichia coli BL21 (DE3). The recombinant E. coli produced a 15-fold higher �\-amylase than B. acidicola strain. The recombinant �\-amylase was purified to homogeneity by one-step nickel affinity chromatography using Ni(2+)-NTA resin with molecular mass of 62 KDa. It is active in the pH range between 3.0 and 7.0 and 30 and 100 �XC with optimum at pH 4.0 and 60 �XC. The enzyme is Ca(2+)-independent with K (m) and k (cat) values (on soluble starch) of 1.6 mg ml(-1) and 108.7 s(-1), respectively. The �\-amylase of B. acidicola is acidstable, high maltose forming and Ca(2+)-independent, and therefore, is a suitable candidate for starch hydrolysis and baking.